Limited proteolysis and amino acid replacements in the effector region of Thermus thermophilus elongation factor Tu

European Journal of Biochemistry

Volumn 239, Issue 2, 1996, Pages 265-271

  Zeidler, Waltraud ^a   Schirmer, Norbert K ^a   Egle, Christian ^a   Ribeiro, Sofia ^a   Kreutzer, Roland ^a   Sprinzl, Mathias ^a  

^a UNIVERSITY OF BAYREUTH   (Germany)

Author keywords

Elongation factor Tu; GTP hydrolysis; Ribosomes; Site directed mutagenesis; Translation

Indexed keywords

ELONGATION FACTOR TU; GUANOSINE TRIPHOSPHATASE;

AMINO ACID SUBSTITUTION; ARTICLE; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN STRUCTURE; RIBOSOME; RNA TRANSLATION; SITE DIRECTED MUTAGENESIS; THERMUS THERMOPHILUS;

THERMUS THERMOPHILUS;

EID: 0030017819     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0265u.x     Document Type: Article

References (50)

1. Adari, H., Lowy, D. R., Willumsen, B. M., Der, C. J. & McCormick, F. (1988) Guanosine triphosphatase activating protein (GAP) interacts with the p21 ras effector binding domain, Science 240, 518-521.
2. Ahmadian, M. R., Kreutzer, R., Blechschmidt, B. & Sprinzl, M. (1995) Site-directed mutagenesis of Thermus thermophilus EF-Tu: the substitution of Thr-62 by serine or alanine, FEBS Lett. 377, 253-257.
3. Ahmadian, M. R., Kreutzer, R. & Sprinzl, M. (1991) Overproduction of the Thermus thermophilus elongation factor Tu in Escherichia coli, Biochimie (Paris) 73, 1037-1043.
4. Arai, K.-I., Kawakita, M. & Kaziro, Y. (1972) Studies on polypeptide elongation factors from Escherichia coli. II. Purification of factors Tu-guanosine diphosphate, Ts, and Tu-Ts, and crystallization of Tu-guanosine diphosphate and Tu-Ts, J. Biol. Chem. 247, 7029-7037.
5. Arai, K. I., Ota, Y., Arai, N., Nakamura, S., Hennecke, C., Oshima, T. & Kaziro, Y. (1978) Studies on polypeptide-chain-elongation factors from an extreme thermophile, Thermus thermophilus HB8, Eur. J. Biochem. 92, 509-519.
6. Berchtold, H., Reshetnikova, L., Reiser, C. O. A., Schirmer, N. K., Sprinzl, M. & Hilgenfeld, R. (1993) Crystal structure of active elongation factor Tu reveals major domain rearrangements, Nature 365, 126-132.
7. Blank, J., Grillenbeck, N. W., Kreutzer, R. & Sprinzl, M. (1995) Overexpression and purification of Thermus thermophilus elongation factors G, Tu, and Ts from Escherichia coli, Protein Expr. Purif. 6, 637-645.
8. Brosius, J. & Holy, A. (1984) Regulation of ribosomal RNA promoters with a synthetic lac operator, Proc. Natl Acad. Sci. USA 81, 6929-6933.
9. Calés. C., Hancock, J. F., Marshall, C. J. & Hall, A. (1988) The cytoplasmic protein GAP is implicated as the target for regulation by the ras gene product, Nature 332, 548-551.
10. h21 and the mechanism of GTP hydrolysis, Science 265, 1405-1412.
11. Duisterwinkel, F. J., de Graaf, J. M., Schretlen, P. J. M., Kraal, B. & Bosch, L. (1981) A mutant elongation factor Tu which does not immobilize the ribosome upon binding of kirromycin, Eur. J. Biochem. 117, 7-12.
12. Fontana, A., Fassina, G., Vita, C., Dalzoppo, D., Zamai, M. & Zambonin, M. (1986) Correlation between sites of limited proteolysis and segmental mobility in thermolysin, Biochemistry 25, 1847-1851.
13. Forchhammer, K., Rucknagel, K.-P. & Böck, A. (1990) Purification and biochemical characterization of SELB, a translational factor involved in selenoprotein synthesis, J. Biol. Chem. 265, 9346-9350.
14. IHS: an experimental and theoretical study, Biochemistry 33, 3237-3244.
15. Gideon, P., John, J., Frech, M., Lautwein, A., Clark, R., Scheffler, J. E. & Wittinghofer, A. (1992) Mutational and kinetic analyses of the GTPase-activating protein (GAP)-p21 interaction: the C-terminal domain of GAP is not sufficient for full activity, Mol. Cell. Biol. 12, 2050-2056.
16. Gillam, I., Millward, S., Blew, D., von Tigerstrom, M., Wimmer, E. & Tener, G. M. (1967) The separation of soluble ribonucleic acids on benzoylated diethylaminoethylcellulose, Biochemistry 6, 3043-3056.
17. Hilgenfeld, R. (1995) How do the GTPases really work? Struct. Biol. 2, 3-6.
18. Jurnak, F. (1985) Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins, Science 230, 32-36.
19. Kjeldgaard, M., Nissen, P., Thirup. S. & Nyborg, J. (1993) The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation, Structure 1, 35-50.
20. Kjeldgaard, M. & Nyborg, J. (1992) Refined structure of elongation factor EF-Tu from Escherichia coli, J. Mol. Biol. 223, 721-742.
21. Kreutzer, R., Kruft, V., Bobkova, E. V., Lavrik, O. I. & Sprinzl, M. (1992) Structure of the phenylalanyl-tRNA synthetase genes from Thermus thermophilus HB8 and their expression in Escherichia coli, Nucleic Acids Res. 20, 4173-4178.
22. Limmer, S., Reiser, C. O. A., Schirmer, N. K., Grillenbeck, N. W. & Sprinzl, M. (1992) Nucleotide binding and GTP hydrolysis by elongation factor Tu from Thermus thermophilus as monitored by proton NMR, Biochemistry 31, 2970-2977.
23. Lyons, J., Landis, C. A., Harsh, G., Vallar, L., Grünewald, K., Feichtinger, H., Duh, Q.-Y., Clark, O. H., Kawasaki, E., Bourne, H. R. & McCormick, F. (1990) Two G protein oncogenes in human endocrine tumors, Science 249, 655-659.
24. Markby, D. W., Onrust, R. & Bourne, H. R. (1993) Separate GTP binding and GTPase activating domains of a Gα subunit, Science 262, 1895-1901.
25. IHs. Trends Biochem. Sci. 18, 250-254.
26. McCormick, F. (1989) ras GTPase activating protein: signal transmitter and signal terminator, Cell 56, 5-8.
27. Mc1 in their amino-acylation by Escherichia coli methionyl-tRNA synthetase, J. Mol. Biol. 229, 26-36.
28. Mesters, J. R., de Graaf, J. M. & Kraal, B. (1993) Divergent effects of fluoroaluminates on the peptide chain elongation factors EF-Tu and EF-G as members of the GTPase superfamily, FEBS Lett. 321, 149-152.
29. Milburn, M. V., Tong, L., de Vos, A. M., Brünger, A., Yanaizumi, Z., Nishimura, S. & Kim, S.-H. (1990) Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins, Science 247, 939-945.
30. Phe, EF-Tu, and a GTP analog, Science 270, 1464-1472.
31. Nock, S., Grillenbeck, N., Ahmadian, M. R., Ribeiro, S., Kreutzer, R. & Sprinzl, M. (1995) Properties of isolated domains of the elongation factor Tu from Thermus thermophilus HB8, Eur. J. Biochem. 234, 132-139.
32. Ott, G., Faulhammer, H. G. & Sprinzl, M. (1989) Interaction of elongation factor Tu from Escherichia coli with aminoacyl-tRNA carrying a fluorescent reporter group on the 3′ terminus, Eur. J. Biochem. 184, 345-352.
33. Ott, G., Jonak, J., Abrahams, I. P. & Sprinzl, M. (1990) The influence of different modifications of elongation factor Tu from Escherichia coli on ternary complex formation investigated by fluorescence spectroscopy, Nucleic Acids Res. 18, 437-441.
34. Pai, E. F., Krengel, U., Petsko, G. A., Goody, R. S., Kabsch, W. & Wittinghofer, A. (1990) Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution: implications for the mechanism of GTP hydrolysis, EMBO J. 9, 2351-2359.
35. Peter, M. E., Schirmer, N. K., Reiser, C. O. A. & Sprinzl, M. (1990) Mapping the effector region in Thermus thermophilus elongation factor Tu, Biochemistry 29, 2876-2884.
36. Rodnina, M. V., Fricke, R., Kuhn, L. & Wintermeyer, W. (1995) Codon-dependent conformational change of elongation factor Tu preceding GTP hydrolysis on the ribosome, EMBO J. 14, 2613-2619.
37. Rodnina, M. V. & Wintermeyer, W. (1995) GTP consumption of elongation factor Tu during translation of heteropolymeric mRNAs, Proc. Natl Acad. Sci. USA 92, 1945-1949.
38. Scarano, G., Krab, I. M., Bocchini, V. & Parmeggiani, A. (1995) Relevance of histidine-84 in the elongation factor Tu GTPase activity and in poly(Phe) synthesis: its substitution by glutamine and alanine, FEBS Lett. 365, 214-218.
39. Sigal, I. S., Gibbs, J. B., D'Alonzo, J. S. & Scolnick, E. M. (1986) Identification of effector residues and neutralizing epitope of Ha-ras-encoded p21, Proc. Natl Acad. Sci. USA 83, 4725-4729.
40. 4, Nature 372, 276-279.
41. Sprinzl, M. (1994) Elongation factor Tu: a regulatory GTPase with an integrated effector, Trends Biochem. Sci. 19, 245-250.
42. Swart, G. W. M. & Parmeggiani, A. (1987) Effects on the mutation Gly222→aspartic acid on the functions of elongation factor Tu, Biochemistry 26, 2047-2054.
43. Tong, L., de Vos, A. M., Milburn, M. V. & Kim, S.-H. (1991) Crystal structures at 2.2 Å resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP, J. Mol. Biol. 217, 503-516.
44. Trahey, M. & McCormick, F. (1987) A cytoplasmic protein stimulates normal N-ras p21 GTPase, but does not affect oncogenic mutants, Science 238, 542-545.
45. Tubulekas, I. & Hughes, D. (1993) A single amino acid substitution in elongation factor Tu disrupts interaction between the ternary complex and the ribosome, J. Bacteriol. 175, 240-250.
46. Wagner, A., Simon, I., Sprinzl, M. & Goody, R. S. (1995) Interaction of guanosine nucleotides and their analogs with elongation factor Tu from Thermus thermophilus, Biochemistry 34, 12 535-12 542.
47. Wittinghofer, A., Frank, R. & Leberman, R. (1980) Composition and properties of trypsin-cleaved elongation factor Tu, Eur. J. Biochem. 108, 423-431.
48. Yanisch-Perron, C., Vieira, J. & Messing, J. (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13-mp18 and pUC19 vectors, Gene (Amst.) 33, 103-119.
49. Zeidler, W., Egle, C., Ribeiro, S., Wagner, A., Katunin, V., Kreutzer, R., Rodnina, M., Wintermeyer, W. & Sprinzl, M. (1995) Site-directed mutagenesis of Thermus thermophilus elongation factor Tu. Replacement of His85, Asp81 and Arg300, Eur. J. Biochem. 229, 596-604.
50. Zubay, G. (1966) Isolation of transfer RNA, in Procedures in nucleic acid research (Cantoni, G. L. & Davies, D. R., eds) pp. 455-460, Harper & Row, New York.